Differential segmental flexibility and reach dictate the antigen binding mode of chimeric IgD and IgM: implications for the function of the B cell receptor.
D000595:Amino Acid Sequence; D000818:Animals; D000918:Antibody Specificity / Q000235:genetics; D001666:Binding Sites, Antibody / Q000235:genetics; D045744:Cell Line, Tumor; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000378:metabolism; D005822:Genetic Vectors; D007072:Immunoglobulin D / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism* / Q000648:ultrastructure; D007075:Immunoglobulin M / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D007700:Kinetics; D051379:Mice; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D009592:Nitrohydroxyiodophenylacetate / Q000276:immunology* / Q000378:metabolism; D011947:Receptors, Antigen, B-Cell / Q000502:physiology*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000378:metabolism* / Q000648:ultrastructure; D013861:Thiocyanates / Q000737:chemistry; D014162:Transfection
D000939:Epitopes; D007072:Immunoglobulin D; D007075:Immunoglobulin M; D011947:Receptors, Antigen, B-Cell; D011993:Recombinant Fusion Proteins; D013861:Thiocyanates; D009592:Nitrohydroxyiodophenylacetate; C031760:thiocyanate